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The effects of energy source and tryptophan on the rate of protein synthesis and on hormones of the entero-insular axis in the piglet

Published online by Cambridge University Press:  09 March 2007

A. A. Ponter ,
N. O. Cortamira ,
B. Seve ,
D. N. Salter  and
L. M. Morgan
A. A. Ponter
Affiliation:
Institute of Grassland and Environmental Research, Church Lane, Shinfield, Reading, RG2 9AQ
N. O. Cortamira
Affiliation:
Institute of Grassland and Environmental Research, Church Lane, Shinfield, Reading, RG2 9AQ
B. Seve
Affiliation:
I.N.R.A., Station de Recherches Porcines, Saint-Gilles, 35590 L'Hermitage, France
D. N. Salter
Affiliation:
Institute of Grassland and Environmental Research, Church Lane, Shinfield, Reading, RG2 9AQ
L. M. Morgan
Affiliation:
School of Biological Sciences, University of Surrey, Guildford, Surrey, GU2 5XH
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Abstract

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The present experiment was designed to study the influence of dietary energy source (fat or carbohydrate) and tryptophan (TRP) on protein synthesis and plasma insulin concentrations in the piglet. Six dietary regimens, based on either a high-fat (F) or a high-carbohydrate (C) diet with three levels of TRP (deficient, 1; adequate, 2; excess, 3), were used. Fractional protein synthesis rate (ks; % per d) was measured in the liver, Longissimus dorsi (LD), Semitendinosus (ST), skin, femur, brain, pancreas, stomach, mucosa of the duodenum and jejunum, and the whole body, using a‘flooding dose’of 3H-phenylalanine. Mean integrated insulin, gastric inhibitory polypeptide (GIP) and glucose concentrations were higher after the C diets compared with the F diets, TRP supplementation globally augmented ks linearly in the liver, ST, skin and whole body, while it had quadratic effects in the LD (ks highest in the TRP-adequate diet groups) and jejunal mucosa (ks lowest in the TRP-adequate diet groups). Pancreatic ks was increased by TRP addition up to a plateau. ks was highest after the F diets in the digestive tissues while in the skin and LD ks was highest after the C diets. Fasting concentrations of gluconeogenic amino acids were lower (and urea higher) with the F than the C diets, suggesting their use as precursors for glucose synthesis. In conclusion, we have confirmed the depressive effects of TRP deficiency on ks, RNA activity and growth. We could not establish a relationship between plasma insulin and muscle ks. This may be related to the way in which we manipulated plasma insulin concentrations.

Keywords

Protein synthesisInsulinTryptophanPiglets
Type
Response of protein synthesis and hormonal status to energy and tryptophan intake
Information
British Journal of Nutrition , Volume 71 , Issue 5 , May 1994 , pp. 661 - 674
Copyright
Copyright © The Nutrition Society 1994

References

Attaix, D. (1988). The influence of age and weaning on protein synthesis in the lamb. PhD Thesis, University Blaise Pascal, Clermont Ferrand.Google Scholar
Brown, J. C. (1974). “Enterogdstrone” and other new gut peptides. Medical Clinics of North America 58, 1347–1358.CrossRefGoogle Scholar
Cortamira, N. O., Seve, B., Lebreton, Y. & Ganier, P. (1991a). Effect of dietary tryptophan on muscle, liver and whole-body protein synthesis in weaned piglets: relationship to plasma insulin. British Journal of Nutrition 66, 423–435.CrossRefGoogle Scholar
Cortamira, O., Stve, B., Ponter, A. & Salter, D. N. (1991 b). The effect of dietdry energy source and level of tryptophan on growth and protein synThesis in different tissues of early-weaned piglets. Proceedings of the 6th International Symposium on Protein and Nutrition, Herning, Denmark, pp. 122–124.Google Scholar
Fernstrom, J. D. & Wurtman, R. J. (1972). Brain serotonin content: physiological regulation by plasma neutral amino acids. Science 178, 414–416.CrossRefGoogle ScholarPubMed
Forbes, J. M. & Blundell, J. E. (1989). Central control of voluntary feed intake. In The Voluntary Food Intake of Pigs. Occasional publication No. 13, British Society of Animal Production, pp. 7–26 [Forbes, J. M., Varley, M. A. and Lawrence, T. L. J., editors]. Haddington: D. and J. Croal Ltd.Google Scholar
Garlick, P. J. & Lobley, G. E. (1987). Dietary intake and protein turnover. In Protein Metabolism and Nutrition, European Association for Animal Production Publication no. 35, pp. 13–21 [Lehman, J., editor]. Rostock: Wilhem-Pieck-Universitat.Google Scholar
Gerich, J. E., Charles, M. A. & Grodsky, G. M. (1976). Regulation of pancreatic insulin and glucagon secretion. Annual Review of Physiology 38, 353–388.CrossRefGoogle ScholarPubMed
lnstitut National de la Recherche Agronomique (1989). L'alimentation des animaux monogastriques, porc, lapin, volailles (The nutrition of simple-stomached animals: pig, rabbit, jowl), 2nd ed. Paris: Institut National de la Recherche Agronomique.Google Scholar
Jefferson, L. S. (1980). Role of insulin in the regulation of protein synThesis. Diabetes 29, 487–496.CrossRefGoogle ScholarPubMed
Jepson, M. M., Bates, P. C. & Millward, D. J. (1988). The role of insulin and thyroid hormones in the regulation of muscle growth and protein turnover in response to dietary protein in the rat. British Journal of Nutrition 59, 397–415.Google ScholarPubMed
Johnson, A., Hurwitz, R. & Kretchmer, N. (1977). Adaptation of rat pancreatic amylase and chymotrypsinogen to changes in diet. Journal of Nutrition 107, 87–96.CrossRefGoogle ScholarPubMed
Kaplan, J. H. & Pitot, H. C. (1970). The regulation of intermediary amino acid metabolism in animal tissues. In Mammalian Protein Metabolism, Vol. IV, pp. 387443 [Munro, H. N., editor]. New York and London: Academic Press.Google Scholar
Krebs, H. A. (1964). The metabolic fate of amino acids. In Mammalian Protein Metabolism, Vol. I, pp. 125–177 [Munro, H. N. and Allison, J. B., editors]. New York and London: Academic Press.CrossRefGoogle Scholar
Lefaucheur, L. (1990). Changes in muscle fiber populations and muscle enzyme activities in the primiparous lactating sow. Reproduction Nutrition Diveloppement 30, 523–531.CrossRefGoogle ScholarPubMed
Lewis, A. J., Peo, E. R., Cunningham, P. J. & Moser, B. D. (1977). Determination of the optimum dietary proportions of lysine and tryptophan for growing pigs based on growth, food intake and plasma metabolites. Journal of Nutrition 107, 1369–1376.CrossRefGoogle ScholarPubMed
McNurlan, M. A., Tomkins, A. M. & Garlick, P. J. (1979). The effect of starvation on the rate of protein synthesis in rat liver and small intestine. Biochemical Journal 178, 373–379.CrossRefGoogle ScholarPubMed
McPhate, G. F. (1986). The effect of ingestion of single amino acids on glucoregulatory hormones in man. MSc Thesis, University of Surrey.Google Scholar
Maxton, D. G., Cynk, E. U., Jenkins, A. P. & Thompson, R. P. H. (1989). Effect of dietary fat on the small intestine. Gut 30, 1252–1255.CrossRefGoogle Scholar
Morgan, L. M., Morris, B. A. & Marks, V. (1978). Radioimmunoassay of gastric inhibitory polypeptide. Annals of Clinical Biochemistry 15, 175–177.CrossRefGoogle ScholarPubMed
Olefsky, J. M. & Saekow, M. (1978). The effects of dietary carbohydrate content on insulin binding and glucose metabolism by isolated rat adipocytes. Endocrinology 103, 2252–2263.CrossRefGoogle ScholarPubMed
Pell, J. D., Gee, J. M., Wortley, G. M. & Johnson, I. T. (1992). Dietary corn oil and guar gum stimulate intestinal crypt proliferation in rats by independent but potentially synergistic mechanisms. Journal of Nutrition 122, 2447–2456.CrossRefGoogle ScholarPubMed
Ponter, A. A., Salter, D. N., Morgan, L. M. & Flatt, P. R. (1991a).The effect of energy source and feeding level on the hormones of the entero-insular axis, and plasma glucose in the growing pig. British Journal of Nutrition 66, 187–197.CrossRefGoogle Scholar
Ponter, A. A., Seve, B., Cortamira, N. O., Salter, D. N. & Morgan, L. M. (1991 b). The effects of energy source and tryptophan level on hormones of the entero-insular axis and glucose in the early weaned pig after an intragastric infusion of glucose1. Proceedings of the Nutrition Society 50, 227A.Google Scholar
Reeds, P. J., Fuller, M. F., Cadenhead, A. & Hay, S. M. (1987). Urea synThesis and leucine turnover in growing pigs: changes during 2 d following the addition of carbohydrate or fat to the diet. British Journal of Nutrition 58, 301–311.CrossRefGoogle ScholarPubMed
Reeds, P. J., Fuller, M. F., Cadenhead, A., Lobley, G.E. & McDonald, J. D. (1981). Effects of changes in the intakes of protein and non-protein energy on whole-body protein turnover in growing pigs. British Journal of Nutrition 45, 539–546.CrossRefGoogle ScholarPubMed
Ross, G. J. S. (1980). Maximum Likelihood Programme (MLP). Rothamstead: Rothamstead Experimental Station.Google Scholar
Séve, B., Meunier-Salaün, M. C., Monnier, M., Colltaux, Y. & Henry, Y. (1991). Impact of dietary tryptophan and behaviour type on growth performance and plasma amino acids of young pigs. Journal of Animal Science 69, 3679–3688.CrossRefGoogle ScholarPubMed
Séve, B., Reeds, P. J., Fuller, M. F., Cadenhead, A. & Hay, S. M. (1986). Protein synThesis and retention in some tissues of the young pig as influenced by dietary protein intake after early weaning. Possible connection to the energy metabolism. Reproduction Nutrition Diveloppement 26, 849–861.CrossRefGoogle Scholar
Sidransky, H., Verney, E. & Sarma, D. S. R. (1971). Effect of tryptophan on polyribosomes and protein synThesis in liver. American Journal of Clinical Nutrition 24, 779–785.CrossRefGoogle ScholarPubMed
Southorn, B. G., Kelly, J. M. & McBride, B. W. (1992). Phenylalanine flooding dose procedure is effective in measuring intestinal and liver protein synThesis in sheep. Journal of Nutrition 122, 2398–2407.CrossRefGoogle ScholarPubMed
Statistical Analysis Systems Institute Inc. (1989). SAS/STST User's Guide, Release 6.03. Cary, NC: SAS Institute Inc.Google Scholar
Stephens, J. R., Woolson, R. F. & Cooke, A. R. (1975). Effects of essential and non essential amino acids on gastric emptying in the dog. Gastroenterology 69, 920–927.CrossRefGoogle Scholar
Sun, J. V., Tepperman, H. M. & Tepperman, J. (1977). A comparison of insulin binding by liver plasma membranes of rats fed a high glucose diet or a high fat diet. Journal of Lipid Research 18, 533–539.CrossRefGoogle ScholarPubMed
Sykes, S., Morgan, L. M., English, J. & Marks, V. (1980). Evidence for preferential stimulation of GIP secretion in the rat by actively transported carbohydrates and their analogues. Journal of Endocrinology 85, 201–207.CrossRefGoogle ScholarPubMed
Thomas, F. B., Sinar, D., Mazzerferri, E. L., Cataland, S., Mekjian, H. S., Caldwell, J. H. & Fromkes, J. J. (1978). Selective release of gastric inhibitory polypeptide by intraduodenal amino acid perfusion in man. Gastroenterology 74, 1261–1265.CrossRefGoogle ScholarPubMed
Tsiolakis, D. & Marks, V. (1984). The differential effect of intragastric and intravenous tryptophan on plasma glucose, insulin, glucagon and GIP in the fasted rat. Hormone and Metabolic Research 16, 226–229.CrossRefGoogle ScholarPubMed
Vesely, J. & Cihak, A. (1970). Enhanced DNA-dependent RNA polymerase and RNA synThesis in rat liver nuclei after administration of L-tryptophan. Biochimica et Biophysica Acta 204, 614–616.CrossRefGoogle ScholarPubMed
Wicker, C. & Puigserver, A. (1987). Effects of inverse changes in dietary lipid and carbohydrate on the synThesis of some pancreatic secretory proteins. European Journal of Biochemistry 162, 25–30.CrossRefGoogle ScholarPubMed
Wicker, C. & Puigserver, A. (1989). Changes in mRNA levels of rat pancreatic lipase in the early days of consumption of a high-lipid diet. European Journal of Biochemistry 180, 563–567.CrossRefGoogle ScholarPubMed
Wittman, J. S. (1975). Alteration of glucose tolerance by dietary L-tryptophan in rats. Journal of Nutrition 106, 631–635.CrossRefGoogle Scholar